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Protein

Polyketide synthase BAS

Gene

BAS

Organism
Rheum palmatum (Chinese rhubarb)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Polyketide synthase producing 4-hydroxybenzalacetone. Can use p-coumaryl-CoA as substrate but does not accept hexanoyl-CoA, isobutyryl-CoA, isovaleryl-CoA, and acetyl-CoA as a substrates. Catalyzes the initial key reaction step in the biosynthesis of phenylbutanoids.2 Publications

Catalytic activityi

4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2.2 Publications

Kineticsi

kcat is 1.79 min(-1) with 4-coumaroyl-CoA as substrate (at pH 8 and 30 degrees Celsius).

  1. KM=10 µM for 4-coumaroyl-CoA (at pH 8 and 30 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 8.0-8.8.2 Publications

    Pathwayi: flavonoid biosynthesis

    This protein is involved in the pathway flavonoid biosynthesis, which is part of Secondary metabolite biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway flavonoid biosynthesis and in Secondary metabolite biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei157Nucleophile and monoketide coumarate intermediate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Chromophore

    Enzyme and pathway databases

    BRENDAi2.3.1.212. 13067.
    UniPathwayiUPA00154.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyketide synthase BAS (EC:2.3.1.212)
    Alternative name(s):
    Benzalacetone synthase
    Short name:
    RpBAS
    Gene namesi
    Name:BAS
    OrganismiRheum palmatum (Chinese rhubarb)
    Taxonomic identifieri137221 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPolygonaceaePolygonoideaeRumiceaeRheum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi190C → G or T: Normal benzalacetone synthase activity. 1 Publication1
    Mutagenesisi207 – 208IL → LF: Acquires an additional chalcone synthase activity. 1 Publication2
    Mutagenesisi249G → L: Reduced benzalacetone synthase activity. 1 Publication1
    Mutagenesisi331S → V: Enhanced benzalacetone synthase activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL1075247.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004242911 – 384Polyketide synthase BASAdd BLAST384

    Keywords - PTMi

    Hydroxylation

    Interactioni

    Subunit structurei

    Homodimer.

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    DIPiDIP-58521N.

    Structurei

    Secondary structure

    1384
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi10 – 18Combined sources9
    Beta strandi23 – 25Combined sources3
    Turni26 – 28Combined sources3
    Helixi29 – 36Combined sources8
    Helixi43 – 54Combined sources12
    Turni55 – 57Combined sources3
    Beta strandi60 – 62Combined sources3
    Helixi67 – 72Combined sources6
    Helixi74 – 77Combined sources4
    Beta strandi78 – 82Combined sources5
    Helixi84 – 110Combined sources27
    Helixi114 – 116Combined sources3
    Beta strandi119 – 126Combined sources8
    Beta strandi129 – 131Combined sources3
    Helixi133 – 140Combined sources8
    Beta strandi148 – 154Combined sources7
    Helixi159 – 173Combined sources15
    Beta strandi178 – 185Combined sources8
    Turni188 – 190Combined sources3
    Helixi204 – 207Combined sources4
    Beta strandi211 – 220Combined sources10
    Turni223 – 225Combined sources3
    Beta strandi230 – 239Combined sources10
    Beta strandi246 – 252Combined sources7
    Beta strandi255 – 260Combined sources6
    Helixi264 – 280Combined sources17
    Helixi281 – 283Combined sources3
    Helixi288 – 290Combined sources3
    Beta strandi291 – 295Combined sources5
    Helixi300 – 310Combined sources11
    Helixi314 – 317Combined sources4
    Helixi318 – 327Combined sources10
    Helixi331 – 333Combined sources3
    Helixi334 – 348Combined sources15
    Turni354 – 357Combined sources4
    Beta strandi359 – 367Combined sources9
    Turni368 – 370Combined sources3
    Beta strandi371 – 379Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3A5QX-ray1.80A/B1-384[»]
    3A5RX-ray1.60A/B1-384[»]
    3A5SX-ray1.80A/B1-384[»]
    ProteinModelPortaliQ94FV7.
    SMRiQ94FV7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ94FV7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chalcone/stilbene synthases family.Curated

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q94FV7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATEEMKKLA TVMAIGTANP PNCYYQADFP DFYFRVTNSD HLINLKQKFK
    60 70 80 90 100
    RLCENSRIEK RYLHVTEEIL KENPNIAAYE ATSLNVRHKM QVKGVAELGK
    110 120 130 140 150
    EAALKAIKEW GQPKSKITHL IVCCLAGVDM PGADYQLTKL LDLDPSVKRF
    160 170 180 190 200
    MFYHLGCYAG GTVLRLAKDI AENNKGARVL IVCSEMTTTC FRGPSETHLD
    210 220 230 240 250
    SMIGQAILGD GAAAVIVGAD PDLTVERPIF ELVSTAQTIV PESHGAIEGH
    260 270 280 290 300
    LLESGLSFHL YKTVPTLISN NIKTCLSDAF TPLNISDWNS LFWIAHPGGP
    310 320 330 340 350
    AILDQVTAKV GLEKEKLKVT RQVLKDYGNM SSATVFFIMD EMRKKSLENG
    360 370 380
    QATTGEGLEW GVLFGFGPGI TVETVVLRSV PVIS
    Length:384
    Mass (Da):42,225
    Last modified:December 1, 2001 - v1
    Checksum:i4068107D7A3EE4B0
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF326911 mRNA. Translation: AAK82824.1.

    Genome annotation databases

    KEGGiag:AAK82824.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF326911 mRNA. Translation: AAK82824.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3A5QX-ray1.80A/B1-384[»]
    3A5RX-ray1.60A/B1-384[»]
    3A5SX-ray1.80A/B1-384[»]
    ProteinModelPortaliQ94FV7.
    SMRiQ94FV7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-58521N.

    Chemistry databases

    ChEMBLiCHEMBL1075247.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAK82824.

    Enzyme and pathway databases

    UniPathwayiUPA00154.
    BRENDAi2.3.1.212. 13067.

    Miscellaneous databases

    EvolutionaryTraceiQ94FV7.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiBAS_RHEPA
    AccessioniPrimary (citable) accession number: Q94FV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: December 1, 2001
    Last modified: November 2, 2016
    This is version 63 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.